ID K2QR36_MACPH Unreviewed; 504 AA.
AC K2QR36;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FAD linked oxidase {ECO:0000313|EMBL:EKG12366.1};
GN ORFNames=MPH_10483 {ECO:0000313|EMBL:EKG12366.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG12366.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG12366.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG12366.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG12366.1}.
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DR EMBL; AHHD01000451; EKG12366.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QR36; -.
DR STRING; 1126212.K2QR36; -.
DR VEuPathDB; FungiDB:MPH_10483; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_2_1; -.
DR InParanoid; K2QR36; -.
DR OrthoDB; 879734at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF34; FAD BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_3G02770); 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..504
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003863339"
FT DOMAIN 70..241
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 504 AA; 55204 MW; FDB4EB704932D2B9 CRC64;
MAALAPSVLL LLLLLLASLQ ASAQFFALPS GRALSSSGCD AACATLASDF GSQLHYPNAD
NFTVWDAKQQ DSHPACRIEP KTTEEVAAVL KVLLDHWCKF AVKSGGHSSS KDASNSVGGV
TVDLKRINQV EVSADKTRTK VGTGAIWGDV YRTLEPDNLG VMGGRVDDVG VGGLLLGGGI
SFLSARYGWA TDNILEVEMV LPNATIITAN EHCNPDLFFA IRGGGNNFGI VTRFTLKTVS
LGKVYGGQKF YSPDKMDALI DASYNLMMSN DPDIAYWTGY IWMPAKNATL ALSQLMYTQD
VKESPAIYSE IDQIEAVGST MRTEYTSNFS MELKQGTPSG HRNWMASMTF TPSKEQERRM
IQIFNEELEI LKVEGKSACP AMTFQPIPVA AIDAMNSRGG NAIGIESDGP LTLMNVATSW
TNVEEDNAVY AYRERLLRRF RESAEELGVL NKYVYMNYAC SQYDDVFSGY KAENVERLKE
IQKRVDPDGV FTSNGLCTGY FKLF
//
